ID A0A1S2ZT21_ERIEU Unreviewed; 1700 AA.
AC A0A1S2ZT21;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
GN Name=XRN1 {ECO:0000313|RefSeq:XP_007524127.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007524127.1};
RN [1] {ECO:0000313|RefSeq:XP_007524127.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR006743}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family.
CC {ECO:0000256|PIRNR:PIRNR006743}.
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DR RefSeq; XP_007524127.1; XM_007524065.2.
DR STRING; 9365.ENSEEUP00000010422; -.
DR CTD; 54464; -.
DR eggNOG; KOG2045; Eukaryota.
DR InParanoid; A0A1S2ZT21; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:InterPro.
DR CDD; cd18673; PIN_XRN1-2-like; 1.
DR Gene3D; 1.25.40.1050; -; 1.
DR Gene3D; 2.170.260.40; -; 1.
DR Gene3D; 2.30.30.750; -; 1.
DR Gene3D; 3.40.50.12390; -; 1.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR016494; 5_3_exoribonuclease_1.
DR InterPro; IPR041385; SH3_12.
DR InterPro; IPR040992; XRN1_D1.
DR InterPro; IPR047007; XRN1_D1_sf.
DR InterPro; IPR041106; XRN1_D2_D3.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR004859; Xrn1_N.
DR InterPro; IPR047008; XRN1_SH3_sf.
DR PANTHER; PTHR12341:SF41; 5'-3' EXORIBONUCLEASE 1; 1.
DR PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR Pfam; PF18129; SH3_12; 1.
DR Pfam; PF18332; XRN1_D1; 1.
DR Pfam; PF18334; XRN1_D2_D3; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF006743; Exonuclease_Xnr1; 2.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR006743};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR006743};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006743};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR006743};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR006743}.
FT DOMAIN 1..227
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 272..594
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 649..841
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 847..1072
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1099..1168
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
FT REGION 1188..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1644..1700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1644..1676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1700 AA; 193262 MW; 0AEB22A3CEC695A2 CRC64;
MGVPKFYRWI SERYPCLSEV VKEHQIPEFD NLYLDMNGII HQCSHPNDDD VHFRISDDKI
FTDIFHYLEV LFRIIKPRKV FFMAVDGVAP RAKMNQQRGR RFRSAKEAED KIKKAIEKGE
TLPTEARFDS NCITPGTEFM ARLHEHLKYF VNMKISTDKS WQGVTIYFSG HETPGEGEHK
IMEFIRSEKA KPDHDPNTRH CLYGLDADLI MLGLTSHEAH FSLLREEVRF GGKKTQRVCA
PEETTFHLLH LSLMREYIDY EFSVLKDKIT FKYDIERIID DWILMGFLVG NDFIPHLPHL
HINHDALPLL YGTYITILPE LGGYINECGH LSLPRFEKYL VKLSDFDREH FSEVFVDLKW
FESKVGNKYL NEAAGVAAEE AKVYKEKKKL KGQENLCWAA LDKKELVTSK DNLEDETEDD
DLFETEFRQY KRTYYMTKMG VDIVSDDFLA DQATCYVQAI QWILHYYYHG VQSWSWYYPY
HYAPFLSDIR NISTLKIHFE LGKPFKPFEQ LLAVLPAASK NLLPVCYQHL MTSEDSPIIE
YYPPDFKTDL NGKQQEWEAV VLIPFIDEKR LLEAMETCNH SLKKEEKKRN QHSECLMCWY
DRDTTFTYPS PWPEKFPAIE RCCTRYKVIS LDAWRVDISK NKITKVDQKA LYFCGFPTLK
HIKHKFFLKK SGVQVFQQSS RGENMMLEIL VNIDSDELSI ENVASSVLGK SVFVNWPHLE
EARVVGVSDG ETKFYLEEPP GTQKLYLGRT APPSKLIHLG DKEQSNWAKE VQGISEYYLR
RKGIMVNETS AVVYAQLLTG RKYQINQNGE VRLEKQWSKQ VLPFVYQTIV KDIRAFDSRF
SSIKTLDDLF PPGSMVFMIG TPYYGCTGEV QDSGDVIAEG RIRVVFSIPC EPTLDALIQN
QHKYSIKYNP GYVLASRLGV SGYLVSRFTG SIFIGRGSRR NPHGDHKANV GLNLKFNKKN
EEVPGYTKKV GSEWMYSSAA EQLLAEYLER APELFSYIAK NSQEDVFYED DIWPGENENG
AEKVQEIITW LKGHPVSTLS RSSCDLQILD AAIVEKIEEE VEKCKQRKNN KKVRVTVKPH
LLYRPLEQQH GVIPDRDAEF RLFDRVVNVR ENFSVPVGLR GTIVGIKGAS READVLFEVL
FDEEFPGGLT IRCSSGRGYR LPTSALVNLS HGSRSETGNQ KLTAIVKPQP SMSHSSSHSS
IPSGHLGGLN HSPQSLFVPT QVSSKDDDEF CNIWQSLQGS RKGQHFQPTL QEKGAVLPQE
ISQVTQHHKS SFSDNIKCQQ RKSEHHGKFK EEYKSSKPDS RPQKMSNKQP SPGIENFLAS
LNILKESEAQ PAHQEEPPTE EHLSPQSFAM KGTRMLKEIL KIDSSDTVDH KNEVKQSGNE
VTISNRKDEY ESSSQPRQNK KLTSSMNKPH STSEYPNIQP VDNVCWPAPN QIPPVTTPVT
ELSRICSLVG MPQPDFSFLR TAQTMTVCQV KLSNGLLVHG PQCHSENEAK EKAAFFALQQ
LGSLGVNFPL PPPIFPNYPA VPPGTIPPVF PQSTGWDHSA NYLALGTANI MSSSPHLFGS
MPWGPPVPVP GKPFHHTSFS GTMPIPGGMP SGVHNQFIPL QVTKKRVANK KNFENKEAHI
SQAIPLQTNQ SAPSDVTKVI PQESAATSFK SSQVTQPASS LQVEAASQGH NMSHHKSNPS
SSRRKTRKLA VNFGVSKPSE
//